Evidence for a high affinity, saturable, prenylation-dependent p21Ha-ras binding site in plasma membranes.
Oncogenic p21ras proteins can only exert their stimulation of cellular proliferation when plasma membrane-associated. This membrane association has an absolute requirement for post-translational modification with isoprenoids. The mechanism by which isoprenoids participate in the specific association of p21ras with plasma membranes is the subject of this report. We present in vitro evidence for a plasma membrane binding protein for p21(ras) that can recognize the isoprenoid substituent and, therefore, may facilitate the localization of p21ras.
Siddiqui
A A
AA
Department of Biochemistry and Molecular Biology, East Tennessee State University, James H. Quillen College of Medicine, Box 70581, Johnson City, Tennessee 37614-0581, USA.
Garland
J R
JR
Dalton
M B
MB
Sinensky
M
M
D016475:3T3 Cells; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002462:Cell Membrane / Q000378:metabolism; D008024:Ligands; D051379:Mice; D008969:Molecular Sequence Data; D017368:Protein Prenylation; D016283:Proto-Oncogene Proteins p21(ras) / Q000378:metabolism*
D008024:Ligands; D016283:Proto-Oncogene Proteins p21(ras)